title: Reconstitution of the pyridoxal 5'-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis.
abstract: The pyridoxal 5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) is required for de novo sphingolipid biosynthesis. A previous study revealed a novel and unexpected interaction between the hydroxyl group of the l-serine substrate and the 5'-phosphate group of PLP. By using pyridoxal (PL), the dephosphorylated analogue of vitamin B6, we show here that this interaction is important for substrate specificity and optimal catalytic efficiency.
authors.affiliation: EaStCHEM, School of Chemistry, University of Edinburgh, Edinburgh, EH9 3JJ, Scotland, UK.
authors.forename: Ashley E
authors.initials: AE
authors.lastname: Beattie
authors.forename: David J
authors.initials: DJ
authors.lastname: Clarke
authors.forename: John M
authors.initials: JM
authors.lastname: Wadsworth
authors.forename: Jonathan
authors.initials: J
authors.lastname: Lowther
authors.forename: Ho-Lam
authors.initials: HL
authors.lastname: Sin
authors.forename: Dominic J
authors.initials: DJ
authors.lastname: Campopiano
mesh_terms: D055162:Biocatalysis; D007700:Kinetics; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D051102:Serine C-Palmitoyltransferase / Q000378:metabolism*; D020578:Sphingomonas / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D012694:Serine; D011732:Pyridoxal Phosphate; D051102:Serine C-Palmitoyltransferase